Purification, crystallization and preliminary X-ray diffraction analysis of the Trichoderma reesei hydrophobin HFBI

Sanna Askolin, Johan P. Turkenburg, Maija Tenkanen, Sinikka Uotila, Keith S. Wilson, Merja Penttilä, Kalevi Visuri

Research output: Contribution to journalArticleScientificpeer-review

8 Citations (Scopus)

Abstract

Hydrophobins are fungal proteins that are capable of altering the hydrophobicity of surfaces by self-assembly at hydrophilic-hydrophobic interfaces. Here, the growth of hydrophobin crystals suitable for X-ray crystallography is reported. The hydrophobin HFBI from Trichoderma reesei was crystallized by vapour diffusion in hanging drops in 30% PEG 4000, 0.1 M sodium citrate pH 4.3 buffer containing 0.2 M ammonium acetate and CYMAL-5 detergent (initial concentration of 2.4 mM). HFBI crystals are hexagonal and belong to space group P61 (or P65), with unit-cell parameters a = b = 45.9, c = 307.2 Å. The HFBI used in the crystallization experiments was purified from fungal cell walls.

Original languageEnglish
Pages (from-to)1903-1905
Number of pages3
JournalActa Crystallographica Section D: Biological Crystallography
Volume60
Issue number10
DOIs
Publication statusPublished - 1 Oct 2004
MoE publication typeA1 Journal article-refereed

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Trichoderma
Crystallization
purification
X-Ray Diffraction
X ray diffraction analysis
Purification
crystallization
detergents
citrates
hydrophobicity
diffraction
crystallography
crystals
self assembly
acetates
Crystals
x rays
Fungal Proteins
buffers
X ray crystallography

Keywords

  • hydrophobins
  • HFBI

Cite this

Askolin, Sanna ; Turkenburg, Johan P. ; Tenkanen, Maija ; Uotila, Sinikka ; Wilson, Keith S. ; Penttilä, Merja ; Visuri, Kalevi. / Purification, crystallization and preliminary X-ray diffraction analysis of the Trichoderma reesei hydrophobin HFBI. In: Acta Crystallographica Section D: Biological Crystallography. 2004 ; Vol. 60, No. 10. pp. 1903-1905.
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abstract = "Hydrophobins are fungal proteins that are capable of altering the hydrophobicity of surfaces by self-assembly at hydrophilic-hydrophobic interfaces. Here, the growth of hydrophobin crystals suitable for X-ray crystallography is reported. The hydrophobin HFBI from Trichoderma reesei was crystallized by vapour diffusion in hanging drops in 30{\%} PEG 4000, 0.1 M sodium citrate pH 4.3 buffer containing 0.2 M ammonium acetate and CYMAL-5 detergent (initial concentration of 2.4 mM). HFBI crystals are hexagonal and belong to space group P61 (or P65), with unit-cell parameters a = b = 45.9, c = 307.2 {\AA}. The HFBI used in the crystallization experiments was purified from fungal cell walls.",
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Purification, crystallization and preliminary X-ray diffraction analysis of the Trichoderma reesei hydrophobin HFBI. / Askolin, Sanna; Turkenburg, Johan P.; Tenkanen, Maija; Uotila, Sinikka; Wilson, Keith S.; Penttilä, Merja; Visuri, Kalevi.

In: Acta Crystallographica Section D: Biological Crystallography, Vol. 60, No. 10, 01.10.2004, p. 1903-1905.

Research output: Contribution to journalArticleScientificpeer-review

TY - JOUR

T1 - Purification, crystallization and preliminary X-ray diffraction analysis of the Trichoderma reesei hydrophobin HFBI

AU - Askolin, Sanna

AU - Turkenburg, Johan P.

AU - Tenkanen, Maija

AU - Uotila, Sinikka

AU - Wilson, Keith S.

AU - Penttilä, Merja

AU - Visuri, Kalevi

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AB - Hydrophobins are fungal proteins that are capable of altering the hydrophobicity of surfaces by self-assembly at hydrophilic-hydrophobic interfaces. Here, the growth of hydrophobin crystals suitable for X-ray crystallography is reported. The hydrophobin HFBI from Trichoderma reesei was crystallized by vapour diffusion in hanging drops in 30% PEG 4000, 0.1 M sodium citrate pH 4.3 buffer containing 0.2 M ammonium acetate and CYMAL-5 detergent (initial concentration of 2.4 mM). HFBI crystals are hexagonal and belong to space group P61 (or P65), with unit-cell parameters a = b = 45.9, c = 307.2 Å. The HFBI used in the crystallization experiments was purified from fungal cell walls.

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